SAXSdb — 2ccl

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1. Protein Identity and Related Structures Protein Identity & Related Structures

CELLULOSOMAL SCAFFOLDING PROTEIN A

CLOSTRIDIUM THERMOCELLUM

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	ENDO-1,4-BETA-XYLANASE Y × 1 （P51584） PHOSPHATE ION × 2 CALCIUM ION × 2 water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	ENDO-1,4-BETA-XYLANASE Y × 1 （P51584） CALCIUM ION × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CIPA_CLOTM
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–150； UniProt 181–328 Author chain C； PDBConstruct 3–150； UniProt 181–328

ENDO-1,4-BETA-XYLANASE Y

CLOSTRIDIUM THERMOCELLUM

UniProt P51584

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	CELLULOSOMAL SCAFFOLDING PROTEIN A × 1 （Q06851） PHOSPHATE ION × 2 CALCIUM ION × 2 water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	CELLULOSOMAL SCAFFOLDING PROTEIN A × 1 （Q06851） CALCIUM ION × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	XYNY_CLOTM
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 2–63； UniProt 730–791 Author chain D； PDBConstruct 2–63； UniProt 730–791

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2ccl
Deposition date deposition_date	2006-01-16
Structure title title	THE S45A, T46A MUTANT OF THE TYPE I COHESIN-DOCKERIN COMPLEX FROM THE CELLULOSOME OF CLOSTRIDIUM THERMOCELLUM
Keywords keywords	;CELL ADHESION, COHESIN-DOCKERIN COMPLEX, CELLULOSOME, COHESIN, DOCKERIN, CLOSTRIDIUM THERMOCELLUM, SCAFFOLDING, CELLULOSE DEGRADATION, HYDROLASE, GLYCOSIDASE ;; CELL ADHESION
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

2ccl__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2ccl__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2ccl__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	19.69 Å
Rg (electron density)	18.74 Å
Total Rg	19.76 Å
Atom count	1595
Residues	211
Excluded volume	28549 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2ccl__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2ccl__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	CELLULOSOMAL SCAFFOLDING PROTEIN A
Molecular weight formula_weight	16956.0 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C
Atom count atom_count	3707

MASDGVVVEIGKVTGSVGTTVEIPVYFRGVPSKGIANCDFVFRYDPNVLEIIGIDPGDIIVDPNPTKSFDTAIYPDRKIIVFLFAEDSGTGAYAITKDGVFAKIRATVKSSAPGYITFDEVGGFADNDLVEQKVSFIDGGVNVGNATPTKLEHHHHHH

Source Source

Source organism organism	CLOSTRIDIUM THERMOCELLUM
NCBI taxonomy ID ncbi_taxonomy_id	1515
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	ENDO-1,4-BETA-XYLANASE Y
Molecular weight formula_weight	6794.9 kDa
EC 编号 ec_number	3.2.1.8
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D

MVLLGDVNGDGTINSTDLTMLKRSVLRAITLTDDAKARADVDKNGSINAADVLLLSRYLLRVI

Source Source

Source organism organism	CLOSTRIDIUM THERMOCELLUM
NCBI taxonomy ID ncbi_taxonomy_id	1515
Host organism host_organism	ESCHERICHIA COLI

Entity 3 Entity 3 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	496

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6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d2ccla2
Class class	b — All beta proteins
Fold Fold fold	b.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamily	b.2.2 — Carbohydrate-binding domain
Family Family family	b.2.2.2 — Cellulose-binding domain family III

Domain ID domain_id	d2ccla3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d2cclb1
Class class	a — All alpha proteins
Fold Fold fold	a.139 — Type I dockerin domain
Superfamily Superfamily superfamily	a.139.1 — Type I dockerin domain
Family Family family	a.139.1.1 — Type I dockerin domain

Domain ID domain_id	d2cclc2
Class class	b — All beta proteins
Fold Fold fold	b.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamily	b.2.2 — Carbohydrate-binding domain
Family Family family	b.2.2.2 — Cellulose-binding domain family III

Domain ID domain_id	d2cclc3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d2ccld_
Class class	a — All alpha proteins
Fold Fold fold	a.139 — Type I dockerin domain
Superfamily Superfamily superfamily	a.139.1 — Type I dockerin domain
Family Family family	a.139.1.1 — Type I dockerin domain

CATH v4.4 (4 domains)

Domain ID domain_id	2cclA01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	680 —

Domain ID domain_id	2cclB00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1330 — Type 1 dockerin domain
Homologous superfamily homologous superfamily	10 — Dockerin domain

Domain ID domain_id	2cclC01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	680 —

Domain ID domain_id	2cclD00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1330 — Type 1 dockerin domain
Homologous superfamily homologous superfamily	10 — Dockerin domain

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Unit-cell length a length_a	48.550 Å
Unit-cell length b length_b	92.647 Å
Unit-cell length c length_c	49.859 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	93.95 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.030 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.1830
R_work r_work	0.1780
R_free r_free	0.2300

THE S45A, T46A MUTANT OF THE TYPE I COHESIN-DOCKERIN COMPLEX FROM THE CELLULOSOME OF CLOSTRIDIUM THERMOCELLUM

1. Protein Identity and Related Structures Protein Identity & Related Structures

CELLULOSOMAL SCAFFOLDING PROTEIN A

State in the Current Structure

Other States of the Same Protein in the Database

ENDO-1,4-BETA-XYLANASE Y

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

2ccl__assembly_1__model_1

2ccl__assembly_1__model_1 | I(q)

2ccl__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (6 domains)

CATH v4.4 (4 domains)

7. Citations (1)

THE S45A, T46A MUTANT OF THE TYPE I COHESIN-DOCKERIN COMPLEX FROM THE CELLULOSOME OF CLOSTRIDIUM THERMOCELLUM

1. Protein Identity and Related Structures Protein Identity & Related Structures

CELLULOSOMAL SCAFFOLDING PROTEIN A

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

ENDO-1,4-BETA-XYLANASE Y

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

2ccl__assembly_1__model_1

2ccl__assembly_1__model_1 | I(q)

2ccl__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (6 domains)

CATH v4.4 (4 domains)

7. Citations (1)